ID   A0A2U9R5M2_PICKU        Unreviewed;      1023 AA.
AC   A0A2U9R5M2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=C5L36_0C05930 {ECO:0000313|EMBL:AWU76667.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU76667.1, ECO:0000313|Proteomes:UP000249293};
RN   [1] {ECO:0000313|EMBL:AWU76667.1, ECO:0000313|Proteomes:UP000249293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS573 {ECO:0000313|EMBL:AWU76667.1,
RC   ECO:0000313|Proteomes:UP000249293};
RA   Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA   Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT   "Population genomics shows no distinction between pathogenic Candida krusei
RT   and environmental Pichia kudriavzevii: One species, four names.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC       of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000256|ARBA:ARBA00007575}.
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DR   EMBL; CP028775; AWU76667.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9R5M2; -.
DR   STRING; 4909.A0A2U9R5M2; -.
DR   VEuPathDB; FungiDB:C5L36_0C05930; -.
DR   OrthoDB; 5477696at2759; -.
DR   Proteomes; UP000249293; Chromosome 3.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000249293}.
FT   DOMAIN          505..755
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
SQ   SEQUENCE   1023 AA;  115303 MW;  9902823FC928F634 CRC64;
     MCPCSSSFQS VYVKQIMLRL LSPKGSGASF TRSYATTASA KLLKKYPLGS EISGYTINRV
     EEIPEFNLVA VALEHQQTGS KHLHVDRQDN NNVFSIIFKT NTPNNTGLPH ILEHTTLCGS
     EKFPVRDPFF KMLNRSLSNF MNAMTGHDYT FYPFATTNVK DFNNLMDIYL DATLHPLLTS
     EDFYQEGWRL ENEITRDKES PLTFKGVVYN EMKGQVSDSS YYFWIKFQES IYPSLNNAGG
     DPSQITQLVH NDLVEFHNKC YHPSNSRTFT YGNIPLAQHL EKLNKVFIPF GKRSNRNILK
     QPIDLNENVK TTIKGPVDPM LPSHQQYKTS LTWKTGSPSD IYETFLLKML SSLLMDGHSS
     PLYQTLVETG LGTDFSVNSG SDSITAANLF TIGLNGLTKD ISDNLEAHIL EVLEAVMKEG
     FADIKIQALI HQLELSRKVE NASFGLNVLS SLVPTWVSNI DPIDSLKWDN IVSRFKEDYS
     KRGDSIFREL LNDKILSKPY FKYTMVPDEI LPSMIAKEEE KRLKDKVDAL SEEDKELIYK
     RGLRLLEKQE EKEDLSCLPT VSVNDIPREF PSVRIDNRVH DGVPIQSRSS PKTNGLSYFR
     ALKTLEASEL PQELIKYLPL FANCLTNMGT KNRSMADLED EIRLYTGGLS CNFFTHASPY
     NTNEVYLKFG LSSVCLNSDF DKMLSLWMQL LLETNFRNVS KLSTLIKLST SDNMSDIVSS
     GHSYARSRAT SKISKVAKIQ ESLGGIANIE FMNELAKLET EGRLEEVVIP KLEKIQQILL
     DGTSLQYSIT TSKDSVGYQE SQIAKFNDDV GFKSNFTKNA YEMPIPATGN LRNEFIQIPS
     HVGFASTALN APSYSSQDSA SLQVLSQLLT FRYLHGEIRE KGGAYGGGAS LDALNGLFTY
     YSYRDPQPLE SLNIYDKAVN VNAYNIKEGV ISDEDLEQAK LTIFQKLEAP KSVRDDGMSY
     FNYDIDDETK QERRGALLDC SLEDVLEVCE KYFPESAVRS KVVIGHDAEG IQGNPNWTTE
     VLK
//